PDB-5byl: Aminoglycoside Phosphotransferase (2'')-Ia (CTD of AAC(6')-Ie/APH...

ID or keywords:

Entry

Database: PDB / ID: 5byl

Title

Aminoglycoside Phosphotransferase (2'')-Ia (CTD of AAC(6')-Ie/APH(2'')-Ia) in complex with GMPPCP and Magnesium

Components

Bifunctional AAC/APH

Keywords

TRANSFERASE / Kinase / Antibiotic / Aminoglycoside / Resistance

Function / homology

Function and homology information

aminoglycoside phosphotransferase activity / aminoglycoside 2''-phosphotransferase / N-acyltransferase activity / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / response to antibiotic / ATP binding / cytoplasm
Similarity search - Function

Biological species

Staphylococcus aureus (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

FOURIER SYNTHESIS / Resolution: 2.15 Å

Authors

Caldwell, S.J. / Berghuis, A.M.

Funding support

Canada, 1items

Citation

Journal: Structure / Year: 2016
Title: Antibiotic Binding Drives Catalytic Activation of Aminoglycoside Kinase APH(2)-Ia.
Authors: Caldwell, S.J. / Huang, Y. / Berghuis, A.M.

History

Deposition	Jun 10, 2015	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	May 25, 2016	Provider: repository / Type: Initial release
Revision 1.1	Jun 15, 2016	Group: Database references
Revision 1.2	Sep 27, 2017	Group: Author supporting evidence / Database references / Derived calculations Category: citation / pdbx_audit_support / pdbx_struct_oper_list Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3	Nov 1, 2017	Group: Author supporting evidence / Category: pdbx_struct_assembly_auth_evidence
Revision 1.4	Jan 8, 2020	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5	Mar 6, 2024	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/by/5byl ftp://data.pdbj.org/pub/pdb/validation_reports/by/5byl	HTTPS FTP

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Related structure data

Related structure data	5iqaC 5iqbC 5iqcC 5iqdC 5iqeC 5iqfC 5iqgC 5iqhC 5iqiC C: citing same article (ref.)
Similar structure data	5iqh-1 6cgg-1 6ch4-3 5iqc-4 6cgg-3 6c5u-3 6cey-1 5iqd-1 5iqa-3 5iqh-2 6ch4-2 6cey-2 6c5u-2 5iqa-2 5iqa-4 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#226 - Oct 2018 Aminoglycoside Antibiotics and Resistance similarity (1) #146 - Feb 2012 Aminoglycoside Antibiotics similarity (5) #97 - Jan 2008 Circadian Clock Proteins similarity (3)

Deposited unit

A: Bifunctional AAC/APH

B: Bifunctional AAC/APH

C: Bifunctional AAC/APH

D: Bifunctional AAC/APH

hetero molecules

147 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Bifunctional AAC/APH

hetero molecules

defined by author&software
Evidence: SAXS
36.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Bifunctional AAC/APH

hetero molecules

defined by author&software
Evidence: SAXS
36.6 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Bifunctional AAC/APH

hetero molecules

defined by author&software
Evidence: SAXS
36.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Bifunctional AAC/APH

hetero molecules

defined by author&software
Evidence: SAXS
36.6 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	90.290, 99.900, 93.620
Angle α, β, γ (deg.)	90.00, 105.09, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
1	2	A
2	2	C
1	3	A
2	3	D
1	4	B
2	4	C
1	5	B
2	5	D
1	6	C
2	6	D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	ALA	ALA	LYS	LYS	A	A	183 - 478	9 - 304
2	1	ALA	ALA	LYS	LYS	B	B	183 - 478	9 - 304
1	2	ALA	ALA	LYS	LYS	A	A	183 - 478	9 - 304
2	2	ALA	ALA	LYS	LYS	C	C	183 - 478	9 - 304
1	3	ALA	ALA	LYS	LYS	A	A	183 - 478	9 - 304
2	3	ALA	ALA	LYS	LYS	D	D	183 - 478	9 - 304
1	4	ASN	ASN	LYS	LYS	B	B	182 - 478	8 - 304
2	4	ASN	ASN	LYS	LYS	C	C	182 - 478	8 - 304
1	5	TYR	TYR	ASP	ASP	B	B	179 - 479	5 - 305
2	5	TYR	TYR	ASP	ASP	D	D	179 - 479	5 - 305
1	6	ASN	ASN	ASP	ASP	C	C	182 - 479	8 - 305
2	6	ASN	ASN	ASP	ASP	D	D	182 - 479	8 - 305

NCS ensembles :

ID
1
2
3
4
5
6

Details

SAXS

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Protein , 1 types, 4 molecules ABCD

#1: Protein	Bifunctional AAC/APH Mass: 35948.199 Da / Num. of mol.: 4 / Fragment: C-terminal domain (UNP residues 175-479) Source method: isolated from a genetically manipulated source Details: C-terminal domain of AAC(6')-Ie/APH(2'')-Ia bifunctional enzyme, residues 175-479 Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: aacA-aphD, R015, VRA0030 / Plasmid: pET-22b-APH(2'')-Ia / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(LDE3) References: UniProt: P0A0C1, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor

#1: Protein

Bifunctional AAC/APH

Mass: 35948.199 Da / Num. of mol.: 4 / Fragment: C-terminal domain (UNP residues 175-479)
Source method: isolated from a genetically manipulated source
Details: C-terminal domain of AAC(6')-Ie/APH(2'')-Ia bifunctional enzyme, residues 175-479
Source: (gene. exp.)

Staphylococcus aureus (bacteria) / Gene: aacA-aphD, R015, VRA0030 / Plasmid: pET-22b-APH(2'')-Ia / Production host:

Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(LDE3)
References: UniProt: P0A0C1, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor

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Non-polymers , 5 types, 1081 molecules

#2: Chemical	ChemComp-GCP / PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER Mass: 521.208 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₁H₁₈N₅O₁₃P₃ / Comment: GMP-PCP, energy-carrying molecule analogue*YM
#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Mg
#4: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Formula: Cl
#5: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₃H₈O₃
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1059 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.84 Å³/Da / Density % sol: 56.62 %
Crystal grow	Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 80-120mM MgCl2, 8% Glycerol, 10% PEG3350, 100mM HEPES pH 7.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
Detector	Type: RAYONIX MX-300 / Detector: CCD / Date: Nov 26, 2013
Radiation	Monochromator: ACCEL/BRUKER double crystal monochromator (DCM), featuring indirectly cryo-cooled first crystal and sagittally focusing second crystal Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9795 Å / Relative weight: 1
Reflection	Resolution: 2.15→58.92 Å / Num. obs: 82837 / % possible obs: 95 % / Redundancy: 3.9 % / R_merge(I) obs: 0.091 / Net I/av σ(I): 3.8 / Net I/σ(I): 12.3
Reflection shell	Resolution: 2.15→2.19 Å / Redundancy: 3.8 % / R_merge(I) obs: 0.532 / Mean I/σ(I) obs: 2.6 / % possible all: 65.6

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0073	refinement
MOSFLM	0.1.27	data reduction
Aimless	0.1.27	data scaling
Coot	0.7.2	model building
REFMAC	5.8.0073	phasing

Refinement

Method to determine structure:

FOURIER SYNTHESIS
Starting model: APH(2'')-Ia GMPPNP-Mg complex

Resolution: 2.15→58.92 Å / Cor.coef. F_o:F_c: 0.97 / Cor.coef. F_o:F_c free: 0.954 / Cross valid method: THROUGHOUT / ESU R: 0.197 / ESU R Free: 0.166 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: Authors state that MG 700 and GCP 500 of chain C have a clash that appears to be a consequence of multiple discrete states in the active site. Refinement of multiple occupancy MG 700 ...

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.19828	4159	5 %	RANDOM
R_work	0.1559	-	-	-
obs	0.15805	78653	94.86 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 47.77 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0 Å²	-0 Å²	0 Å²
2-	-	-0 Å²	-0 Å²
3-	-	-	-0 Å²

Refinement step

Cycle: LAST / Resolution: 2.15→58.92 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9741	0	176	1059	10976

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.016	0.019	10202
X-RAY DIFFRACTION	r_bond_other_d	0	0.02	9305
X-RAY DIFFRACTION	r_angle_refined_deg	1.582	1.97	13829
X-RAY DIFFRACTION	r_angle_other_deg	3.576	3	21511
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.747	5	1211
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.214	25.673	550
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	12.548	15	1834
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.056	15	34
X-RAY DIFFRACTION	r_chiral_restr	0.096	0.2	1504
X-RAY DIFFRACTION	r_gen_planes_refined	0.008	0.02	11744
X-RAY DIFFRACTION	r_gen_planes_other	0.016	0.02	2306
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	2.273	2.744	4766
X-RAY DIFFRACTION	r_mcbond_other	2.273	2.743	4765
X-RAY DIFFRACTION	r_mcangle_it	3.197	4.095	5952
X-RAY DIFFRACTION	r_mcangle_other	3.197	4.096	5953
X-RAY DIFFRACTION	r_scbond_it	3.342	3.146	5436
X-RAY DIFFRACTION	r_scbond_other	3.341	3.146	5436
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	5.12	4.571	7861
X-RAY DIFFRACTION	r_long_range_B_refined	8.568	24.338	12833
X-RAY DIFFRACTION	r_long_range_B_other	8.565	24.215	12778
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	A	18129	0.09
1	2	B	18129	0.09
2	1	A	18197	0.09
2	2	C	18197	0.09
3	1	A	18034	0.09
3	2	D	18034	0.09
4	1	B	17997	0.1
4	2	C	17997	0.1
5	1	B	18453	0.08
5	2	D	18453	0.08
6	1	C	17824	0.1
6	2	D	17824	0.1

LS refinement shell

Resolution: 2.15→2.206 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.271	210	-
R_work	0.241	4101	-
obs	-	-	67.1 %

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	3.5204	-2.6004	4.1154	12.0556	-5.1868	5.2743	0.3164	0.208	0.0995	-0.5856	-0.294	0.6041	0.4264	0.2802	-0.0224	0.1507	0.0181	-0.0078	0.1985	0.0102	0.053	46.273	-3.044	55.546
2	11.4717	14.2154	-2.7683	17.65	-2.9615	8.2183	0.0516	0.0835	0.2343	0.0352	0.0471	0.3325	-0.1847	-0.846	-0.0987	0.3173	0.0794	-0.0575	0.3523	-0.0272	0.3874	45.515	-1.901	36.073
3	1.3274	0.3257	0.372	2.2659	-0.9816	6.7035	0.0088	0.085	0.1785	-0.29	-0.1763	-0.1977	0.0987	0.6337	0.1675	0.0578	0.0321	0.0459	0.2183	-0.0059	0.0878	54.785	2.271	51.355
4	8.2416	1.1743	-1.8665	0.2139	-0.6365	4.1878	0.0204	-0.0019	-0.3887	0.0109	0.0457	0.0088	0.0727	-0.4035	-0.0661	0.2488	0.0049	0.026	0.2063	0.0269	0.2723	41.828	-0.033	50.066
5	8.4143	-6.5576	1.7604	5.1304	-1.1153	4.2066	-0.2182	-0.23	-0.2064	0.1219	0.1402	0.1634	-0.4091	-0.702	0.0779	0.3008	-0.0448	0.0005	0.252	0.0041	0.2836	42.415	13.529	52.747
6	2.3845	-1.0241	-0.2911	5.3661	-1.0984	2.5806	0.0809	0.0618	-0.1197	-0.0564	-0.0836	0.2728	0.088	-0.0225	0.0027	0.0112	-0.0165	-0.0024	0.0707	-0.0095	0.0169	45.962	-6.143	70.845
7	4.4687	-2.1703	1.0392	2.0592	-0.6861	1.3397	-0.0407	-0.0307	0.1702	0.1693	0.0606	0.0861	-0.2885	0.0773	-0.0198	0.0983	-0.0216	0.0647	0.0357	-0.0232	0.116	29.028	11.138	70.833
8	10.0913	3.962	-3.3211	6.4236	-2.6019	6.2159	-0.0884	0.4257	-0.1984	-0.4751	0.1256	-0.2342	0.2558	0.0366	-0.0371	0.1149	0.0482	0.0325	0.1081	-0.0655	0.1282	24.249	6.487	58.576
9	5.1651	2.3825	-0.1578	1.1542	-0.2312	0.4786	0.1549	-0.6588	-0.3353	0.1062	-0.2425	-0.1784	-0.128	-0.1237	0.0876	0.2109	0.0278	-0.0135	0.2299	0.0092	0.1279	37.003	4.539	20.812
10	2.3223	0.8396	-1.1399	0.3105	-0.4149	0.5653	0.0092	-0.0895	-0.1849	0.0106	-0.0639	-0.0317	-0.0128	0.0259	0.0548	0.3669	-0.0008	-0.0058	0.3461	-0.0087	0.3073	37.557	2.766	41.239
11	2.1759	0.1172	0.7689	1.5713	-0.4087	6.7503	-0.1268	-0.252	0.2854	0.2079	0.0216	-0.0389	-0.6448	0.0357	0.1053	0.2601	0.0565	-0.0232	0.0464	-0.0301	0.1003	43.134	12.968	23.893
12	0.0205	0.1696	0.064	6.1058	-0.8335	2.1256	0.0188	-0.0192	-0.0277	-0.01	-0.1219	0.8197	0.1389	-0.1966	0.1032	0.2268	0.0105	-0.0344	0.2158	-0.0216	0.4337	39.862	0.399	27.087
13	3.5188	-0.0086	2.9943	0.0111	-0.3938	17.9392	-0.3048	0.0207	-0.0016	-0.0109	-0.0169	-0.0079	0.5041	0.074	0.3218	0.3239	0.0537	0.035	0.2567	-0.0006	0.2959	53.093	0.624	23.798
14	5.3334	-1.434	0.7118	2.6487	0.0606	1.9194	-0.1439	0.0929	-0.2008	0.0228	0.1582	0.257	-0.0412	-0.1992	-0.0142	0.0644	0.0164	-0.0014	0.0518	0.0131	0.0272	33.754	2.796	5.64
15	1.9369	-1.4075	0.1357	4.7682	-1.106	1.1519	0.0863	0.1148	-0.0958	-0.0889	-0.1053	-0.0515	-0.1248	0.0506	0.0189	0.0325	-0.0111	0.0156	0.0253	-0.0337	0.0566	49.908	-15.167	7.822
16	6.039	3.5647	2.2436	10.0294	2.5124	6.4231	0.2088	-0.4225	0.2921	0.6309	-0.2635	0.6824	-0.0963	-0.4284	0.0547	0.0896	0.0152	0.0859	0.0827	-0.0295	0.1196	44.642	-18.527	20.433
17	5.9548	1.5359	3.5237	1.4102	2.7355	5.4335	0.1325	0.6666	-0.0532	-0.1134	-0.1124	-0.0511	-0.1743	-0.1741	-0.0201	0.1105	0.0383	0.0665	0.2044	-0.075	0.2121	64.622	35.556	74.739
18	3.4234	3.7513	-0.5792	8.1304	5.3304	9.0007	-0.0207	0.1421	-0.4274	-0.2754	0.3447	-0.8236	-0.3319	0.2365	-0.324	0.3728	-0.0423	0.0053	0.4381	0.0205	0.4885	66.705	34.919	55.487
19	2.1959	-0.3138	-0.4925	2.0235	0.7582	8.3029	-0.0639	0.2109	-0.1416	-0.4105	-0.0468	0.0554	0.2655	-0.5843	0.1107	0.117	-0.0535	-0.0162	0.2124	-0.0426	0.1719	56.399	30.088	70.629
20	13.9385	-8.049	2.0443	5.6262	-2.3796	7.3018	-0.2474	-0.4174	0.52	-0.1076	0.2949	-0.738	0.1175	0.1856	-0.0475	0.2704	-0.0346	0.0735	0.2103	-0.0341	0.3213	69.481	32.42	69.112
21	0.6637	2.6312	0.7643	10.5361	3.0361	0.8812	0.0644	0.0042	0.0688	0.266	-0.1465	0.3872	0.0892	-0.0034	0.082	0.3627	0.0714	-0.0056	0.4273	-0.0084	0.3364	67.071	18.691	72.853
22	2.4504	-1.2902	0.7921	3.4751	-1.92	4.3271	-0.113	-0.0747	0.2326	0.1317	-0.0098	-0.1221	-0.3584	-0.1061	0.1228	0.0343	0.0266	-0.0212	0.0955	-0.0633	0.1356	64.515	39.343	89.879
23	4.3765	-1.9484	-1.4657	2.3054	0.6803	1.7513	-0.1743	-0.1383	-0.2868	-0.0418	0.0716	0.1501	0.2101	-0.1137	0.1027	0.0359	-0.0147	0.0138	0.025	0.0113	0.0652	82.058	22.325	91.412
24	9.7407	3.4554	1.8085	7.2924	2.3956	7.1658	-0.1433	0.3744	0.2345	-0.366	-0.0361	0.4626	-0.0564	-0.4622	0.1794	0.0612	0.0238	0.0178	0.0711	0.0208	0.0689	86.986	26.128	79.125
25	10.3633	2.6236	-0.2653	0.8993	0.7046	2.5708	0.0107	-0.6614	0.0055	0.047	-0.1639	0.0497	0.1117	-0.042	0.1533	0.2099	0.0166	0.0192	0.2299	0.0132	0.1322	74.568	28.921	40.418
26	1.6385	2.0197	1.4244	2.5791	1.7795	1.2531	0.1691	-0.3211	0.2579	0.1143	-0.3715	0.0991	0.0585	-0.2601	0.2024	0.6002	-0.0579	0.0071	0.6433	0.0337	0.7409	73.653	29.652	60.796
27	2.1983	-0.3181	-0.7843	2.0892	-0.457	6.8461	-0.1768	-0.2738	-0.3766	0.0181	-0.0268	0.0656	0.363	-0.1042	0.2036	0.1633	-0.0401	0.0416	0.1954	0.0095	0.2753	68.598	20.2	42.946
28	0.7882	-0.7778	1.3784	8.0626	-1.0856	5.1012	0.034	-0.0415	0.5584	-0.4476	-0.238	-1.0613	-0.2752	0.1331	0.2041	0.3538	-0.0437	0.1129	0.3678	-0.0097	0.6635	71.591	32.64	46.689
29	1.751	-5.7106	-14.3138	18.6509	46.3421	121.5615	-0.0794	-0.0474	-0.0138	0.3261	0.1958	0.0552	-0.1701	-0.0006	-0.1164	0.2373	0.0201	0.0439	0.4848	-0.0519	0.3496	58.716	30.739	43.522
30	5.7616	-0.1794	0.327	2.2741	-1.2447	2.26	-0.0434	0.2066	-0.0789	-0.1868	-0.0745	-0.2311	0.1566	0.1618	0.1178	0.117	-0.0182	0.0795	0.1732	-0.0627	0.1042	78.19	31.658	25.529
31	4.459	-2.6228	-0.8525	4.471	0.01	1.5669	-0.1464	0.0489	0.4085	0.215	0.1579	-0.1443	-0.0657	-0.0169	-0.0116	0.097	-0.0207	-0.0605	0.2259	0.0503	0.1496	61.559	49.093	28.231
32	11.3105	4.9897	-3.9404	8.9691	-0.7904	7.2851	-0.179	-0.5408	0.3681	0.7767	0.1177	-0.6639	-0.1505	0.7333	0.0614	0.4131	0.1604	-0.1787	0.5041	-0.0289	0.3031	66.797	52.212	40.705

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	500
2	X-RAY DIFFRACTION	1	A	700 - 702
3	X-RAY DIFFRACTION	1	A	900 - 911
4	X-RAY DIFFRACTION	2	A	183 - 187
5	X-RAY DIFFRACTION	3	A	188 - 207
6	X-RAY DIFFRACTION	3	A	217 - 229
7	X-RAY DIFFRACTION	3	A	237 - 277
8	X-RAY DIFFRACTION	4	A	208 - 216
9	X-RAY DIFFRACTION	5	A	230 - 236
10	X-RAY DIFFRACTION	6	A	278 - 318
11	X-RAY DIFFRACTION	6	A	367 - 431
12	X-RAY DIFFRACTION	7	A	319 - 366
13	X-RAY DIFFRACTION	7	A	432 - 447
14	X-RAY DIFFRACTION	8	A	448 - 479
15	X-RAY DIFFRACTION	9	B	500
16	X-RAY DIFFRACTION	9	B	700 - 702
17	X-RAY DIFFRACTION	9	B	900 - 911
18	X-RAY DIFFRACTION	10	B	179 - 187
19	X-RAY DIFFRACTION	11	B	188 - 207
20	X-RAY DIFFRACTION	11	B	217 - 229
21	X-RAY DIFFRACTION	11	B	237 - 277
22	X-RAY DIFFRACTION	12	B	208 - 216
23	X-RAY DIFFRACTION	13	B	230 - 236
24	X-RAY DIFFRACTION	14	B	278 - 318
25	X-RAY DIFFRACTION	14	B	367 - 431
26	X-RAY DIFFRACTION	15	B	319 - 366
27	X-RAY DIFFRACTION	15	B	432 - 447
28	X-RAY DIFFRACTION	16	B	448 - 479
29	X-RAY DIFFRACTION	17	C	500
30	X-RAY DIFFRACTION	17	C	700 - 702
31	X-RAY DIFFRACTION	17	C	900 - 911
32	X-RAY DIFFRACTION	18	C	182 - 187
33	X-RAY DIFFRACTION	19	C	188 - 207
34	X-RAY DIFFRACTION	19	C	217 - 229
35	X-RAY DIFFRACTION	19	C	237 - 277
36	X-RAY DIFFRACTION	20	C	208 - 216
37	X-RAY DIFFRACTION	21	C	230 - 236
38	X-RAY DIFFRACTION	22	C	278 - 318
39	X-RAY DIFFRACTION	22	C	367 - 431
40	X-RAY DIFFRACTION	23	C	319 - 366
41	X-RAY DIFFRACTION	23	C	432 - 447
42	X-RAY DIFFRACTION	24	C	448 - 479
43	X-RAY DIFFRACTION	25	D	500
44	X-RAY DIFFRACTION	25	D	700 - 702
45	X-RAY DIFFRACTION	25	D	900 - 911
46	X-RAY DIFFRACTION	26	D	179 - 187
47	X-RAY DIFFRACTION	27	D	188 - 207
48	X-RAY DIFFRACTION	27	D	217 - 229
49	X-RAY DIFFRACTION	27	D	237 - 277
50	X-RAY DIFFRACTION	28	D	208 - 216
51	X-RAY DIFFRACTION	29	D	230 - 236
52	X-RAY DIFFRACTION	30	D	278 - 318
53	X-RAY DIFFRACTION	30	D	367 - 431
54	X-RAY DIFFRACTION	31	D	319 - 366
55	X-RAY DIFFRACTION	31	D	432 - 447
56	X-RAY DIFFRACTION	32	D	448 - 479

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